The role of network creation and actor engagement in the adoption and diffusion of sustainable innovations in food value chains

The paper aims at understanding how innovations, that are promoted and facilitated by private actors, can be fostered by network creation and actor engagement in the agri-food value chains. More specifically, we investigated innovative governance mechanisms related to the introduction of new sustainable practices in food value chains and tried to evaluate the environmental, economic and social effects of these new practices. We use information derived from a case study based on an ongoing project in the North of Italy, where in 2013 a multinational corporation operating in the pasta and bakery sector has initiated an agreement with other three agri-food companies in order to facilitate sustainable sourcing from a group of farmers

Limited proteolysis of a disulfide-linked apoA-I dimer in reconstituted HDL.

The apolipoprotein A-I Milano (apoA-I M ) is a mo- lecular variant of apoA-I characterized by the Arg 173 → Cys substitution, leading to the formation of homodimers A-I M / A-I M. Upon interaction with palmitoyloleoylphosphatidyl- choline, A-I M /A-I M forms only two species of reconstituted HDL (rHDL) particles, with diameters of 7.8 and 12.5 nm. We used limited proteolysis to analyze the conformation of A-I M /A-I M in the two rHDL particles, in comparison with that of apoA-I in rHDL of similar size. ApoA-I in the small, 7.8-nm rHDL is degraded to a greater extent (50% after 6 h) than in the large rHDL ( � 10% degraded after 6 h). The pro- tease susceptibility of A-I M /A-I M in small and large rHDL is instead remarkably the same, with A-I M /A-I M being much more sensitive to proteolytic digestion (50% degraded after 10 min) than apoA-I. The identification of the proteolytic fragments by immunoblotting, N-terminal sequencing, and molecular mass determination, shows that the N-terminus of both proteins is resistant to proteolysis, with six cleavage sites located in the central and carboxy-terminal portions of the molecules. Cleavage in the middle of apoA-I occurs at dis- tinct sites in 7.8-nm (Lys 118 ) and 12.7-nm (Arg 123 ) rHDL, in- dicating a different conformation in small and large rHDL particles. The A-I M /A-I M instead adopts a unique and identi- cal conformation in small and large rHDL, with the carboxy- terminal portion of the molecule being remarkably more ac- cessible to the proteases than in apoA-I. This suggests the presence of a novel carboxy-terminal domain in A-I M /A-I M , not organized in a compact structure and not shared by wild-type apoA-I, which may account for the unique functional proper- ties of A-I M /A-I M. —Calabresi, L., G. Tedeschi, C. Treu, S. Ron- chi, D. Galbiati, S. Airoldi, C. R. Sirtori, Y. Marcel, and G. Franceschini. Limited proteolysis of a disulfide-linked apoA-I dimer in reconstituted HDL. J. Lipid Res. 2001. 42: 935-942

ASPIS, A Flexible Multispectral System for Airborne Remote Sensing Environmental Applications

Airborne multispectral and hyperspectral remote sensing is a powerful tool for environmental monitoring applications. In this paper we describe a new system (ASPIS) composed by a 4-CCD spectral sensor, a thermal IR camera and a laser altimeter that is mounted on a flexible Sky-Arrow airplane. A test application of the multispectral sensor to estimate durum wheat quality is also presented